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Reviewed, UniProtKB/Swiss-Prot P10968 (AGI1_WHEAT)

Last modified June 16, 2009. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Agglutinin isolectin 1
Alternative name(s):
    WGA1
    Isolectin A
OrganismTriticum aestivum (Wheat)
Taxonomic identifier4565 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum

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Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding lectin.

Subunit structure

Homodimer, u-shaped.

Miscellaneous

The 4 sites proposed for binding to carbohydrates (N-acetyl-D-glucosamine) of receptor molecules are on the surface of the agglutinin molecule.

Sequence similarities

Contains 4 chitin-binding type-1 domains.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.2
Chain27 – 197171Agglutinin isolectin 1
PRO_0000005255
Propeptide198 – 21215
PRO_0000005256

Regions

Domain27 – 6842Chitin-binding type-1 1
Domain69 – 11143Chitin-binding type-1 2
Domain112 – 15443Chitin-binding type-1 3
Domain155 – 19743Chitin-binding type-1 4
Region36 – 383Substrate binding
Region88 – 9912Substrate binding
Region140 – 1412Substrate binding

Amino acid modifications

Disulfide bond29 ↔ 44
Disulfide bond38 ↔ 50
Disulfide bond43 ↔ 57
Disulfide bond61 ↔ 66
Disulfide bond72 ↔ 87
Disulfide bond81 ↔ 93
Disulfide bond86 ↔ 100
Disulfide bond104 ↔ 109
Disulfide bond115 ↔ 130
Disulfide bond124 ↔ 136
Disulfide bond129 ↔ 143
Disulfide bond147 ↔ 152
Disulfide bond158 ↔ 173
Disulfide bond167 ↔ 179
Disulfide bond172 ↔ 186
Disulfide bond190 ↔ 195

Experimental info

Sequence conflict631N → D Ref.2
Sequence conflict631N → D Ref.3

Secondary structure

1 ................................. 212
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P10968-1 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: EC7B6F007DDC15EB

FASTA21221,239
        10         20         30         40         50         60 
MKMMSTRALA LGAAAVLAFA AATAQAQRCG EQGSNMECPN NLCCSQYGYC GMGGDYCGKG 

        70         80         90        100        110        120 
CQNGACWTSK RCGSQAGGAT CTNNQCCSQY GYCGFGAEYC GAGCQGGPCR ADIKCGSQAG 

       130        140        150        160        170        180 
GKLCPNNLCC SQWGFCGLGS EFCGGGCQSG ACSTDKPCGK DAGGRVCTNN YCCSKWGSCG 

       190        200        210 
IGPGYCGAGC QSGGCDGVFA EAITANSTLL QE

« Hide

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References

[1]"Nucleotide sequences of cDNA clones encoding wheat germ agglutinin isolectins A and D."
Smith J.J., Raikhel N.V.
Plant Mol. Biol. 13:601-603(1989) [PubMed: 2491677] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence variability in three wheat germ agglutinin isolectins: products of multiple genes in polyploid wheat."
Wright C.S., Raikhel N.V.
J. Mol. Evol. 28:327-336(1989) [PubMed: 2499688] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-197.
Tissue: Germ.
[3]"Comparison of the refined crystal structures of two wheat germ isolectins."
Wright C.S.
J. Mol. Biol. 209:475-487(1989) [PubMed: 2585496] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[4]"2.2-A resolution structure analysis of two refined N-acetylneuraminyl-lactose-wheat germ agglutinin isolectin complexes."
Wright C.S.
J. Mol. Biol. 215:635-651(1990) [PubMed: 2231724] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH N-ACETYLNEURAMINYL-LACTOSE.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M25536 mRNA. Translation: AAA34256.1.
PIRS09623.
UniGeneTa.12645

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1WGCX-ray2.20A/B28-197[»]
2CWGX-ray2.00A/B28-197[»]
2UVOX-ray1.40A/B/E/F28-197[»]
2UWGX-ray1.60A/B28-197[»]
7WGAX-ray2.00A/B28-197[»]
ModBaseSearch...

Protein family/group databases

CAZyCBM18. Carbohydrate-Binding Module Family 18.

Organism-specific databases

GrameneP10968.

Family and domain databases

InterProIPR018371. Chitin-binding_1_CS.
IPR001002. Chitin_bd_1.
IPR000726. Glyco_hydro_19_cat.
[Graphical view]
Gene3DG3DSA:3.30.60.10. Chitin_bd_1. 4 hits.
PANTHERPTHR22595. Glyco_hydro_19_cat. 1 hit.
PfamPF00187. Chitin_bind_1. 4 hits.
[Graphical view]
PRINTSPR00451. CHITINBINDNG.
ProDomPD000609. Chitin_binding_1. 3 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00270. ChtBD1. 4 hits.
[Graphical view]
PROSITEPS00026. CHIT_BIND_I_1. 4 hits.
PS50941. CHIT_BIND_I_2. 4 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAGI1_WHEAT
AccessionPrimary (citable) accession number: P10968
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1990
Last modified: June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents